Figure 2 | Scientific Reports

Figure 2

From: Antirepressor specificity is shaped by highly efficient dimerization of the staphylococcal pathogenicity island regulating repressors: Stl repressor dimerization perturbed by dUTPases

Figure 2

Sequence alignment of Stl master repressor proteins of S. aureus SaPIbov1 (Sa-Stl) and S. hominis ShoCI794_SEPI (Sho-Stl) pathogenicity islands. Identical residues are marked with a star (*), strongly similar ones denoted with a colon (:) weakly similar residues marked with a dot (.). Residues constituting the DNA binding helix-turn-helix motif are underlined. Sa-Stl residues interacting the human dUTPase based on crystal structure of the Sa-Stl:human dUTPase complex (PDB ID: 7PWJ) are with bold red letters. Residues on the dimer interface of Sa-Stl (PDB ID: 6H48) are with bold blue letters and those of Sho-Stl (modelled in this study by Alphafold2) interface identified are colored blue (both based on by LigPlot + analysis). Sho-Stl residues which were mutated in this study (K99N, E100D, F105Y) are framed.

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